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SCP26_ARATH
ID   SCP26_ARATH             Reviewed;         452 AA.
AC   Q9ZQQ0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Serine carboxypeptidase-like 26;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL26; OrderedLocusNames=At2g35780; ORFNames=T20F21.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clone.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=15908604; DOI=10.1104/pp.104.057950;
RA   Fraser C.M., Rider L.W., Chapple C.;
RT   "An expression and bioinformatics analysis of the Arabidopsis serine
RT   carboxypeptidase-like gene family.";
RL   Plant Physiol. 138:1136-1148(2005).
CC   -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AC006068; AAM15111.1; -; Genomic_DNA.
DR   EMBL; AC007017; AAD21479.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09160.1; -; Genomic_DNA.
DR   EMBL; AY088044; AAM65590.1; -; mRNA.
DR   EMBL; BT029178; ABJ17113.1; -; mRNA.
DR   PIR; H84772; H84772.
DR   RefSeq; NP_181121.1; NM_129136.5.
DR   AlphaFoldDB; Q9ZQQ0; -.
DR   SMR; Q9ZQQ0; -.
DR   STRING; 3702.AT2G35780.1; -.
DR   ESTHER; arath-SCP26; Carboxypeptidase_S10.
DR   MEROPS; S10.A43; -.
DR   PaxDb; Q9ZQQ0; -.
DR   PRIDE; Q9ZQQ0; -.
DR   ProteomicsDB; 232939; -.
DR   EnsemblPlants; AT2G35780.1; AT2G35780.1; AT2G35780.
DR   GeneID; 818150; -.
DR   Gramene; AT2G35780.1; AT2G35780.1; AT2G35780.
DR   KEGG; ath:AT2G35780; -.
DR   Araport; AT2G35780; -.
DR   TAIR; locus:2039275; AT2G35780.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q9ZQQ0; -.
DR   OMA; YTVTCKK; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q9ZQQ0; -.
DR   PRO; PR:Q9ZQQ0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZQQ0; baseline and differential.
DR   Genevisible; Q9ZQQ0; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..452
FT                   /note="Serine carboxypeptidase-like 26"
FT                   /id="PRO_0000274641"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..338
FT                   /evidence="ECO:0000250"
FT   DISULFID        244..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..306
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   452 AA;  51521 MW;  BA25B878273C470F CRC64;
     MARLLLLFFF FLILLHYASC SRHEQEKDRI FHLPGEPNDV SFSHFSGYIT VNESAGRALF
     YWLTESPPSE NPESKPLVLW LNGGPGCSSV AYGAAEEIGP FRINPDGKTL YHNPYSWNKL
     ANLLFLESPA GVGFSYSNTT SDLYTAGDQR TAEDAYVFLV KWFERFPQYK HREFYIAGES
     YAGHYVPQLS QIVYEKRNPA INFKGFIVGN AVIDDYHDYV GLFEYWWAHG LISDLTYHNL
     RITCEFGSSE HPSSKCTKAM EAADLEQGNI DPYSIYTVTC KKEAAALRSR FSRVRHPWMW
     RAYDPCTEKY SGMYFNSPEV QKAMHANITG LAYPWKGCSD IVGEKWADSP LSMLPIYKEL
     IAAGLRIWVF SGDTDSVVPI TGTRYSIRAL KLQPLSKWYP WNDDGQVGGW SQVYKGLTLV
     TIHGAGHEVP LFRPRRAFLL FQSFLDNKPL PM
 
 
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